Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2.

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Suzuki H, Kawasaki M, Kakiuchi T, Shibata H, Wakatsuki S, Maki M

Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):974-7. doi: 10.1107/S1744309108030297. Epub 2008 Oct 31.

PubMed ID
18997320 [ View in PubMed
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Abstract

ALG-2 (apoptosis-linked gene 2) is an apoptosis-linked calcium-binding protein with five EF-hand motifs in the C-terminal region. N-terminally truncated ALG-2 (des3-23ALG-2) was crystallized by the vapour-diffusion method in buffer consisting of either 50 mM MES pH 6.5, 12.5%(v/v) 2-propanol and 150 mM calcium acetate or 100 mM MES pH 6.0, 15%(v/v) ethanol and 200 mM zinc acetate. Crystals of the Ca(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.8, b = 154.4, c = 237.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.1 A resolution. Crystals of the Zn(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.8, b = 147.5, c = 230.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.3 A resolution. The structures of the Ca(2+)-bound form and the Zn(2+)-bound form were solved by the molecular-replacement method. Although both crystals contained eight ALG-2 molecules per asymmetric unit, the metal-ion locations and octameric arrangements were found to be significantly different.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
CalciumProgrammed cell death protein 6ProteinHumans
Unknown
Not AvailableDetails
ZincProgrammed cell death protein 6ProteinHumans
Unknown
Not AvailableDetails
Zinc acetateProgrammed cell death protein 6ProteinHumans
Unknown
Not AvailableDetails